title: ¹H, ¹³C and ¹⁵N resonance assignments for the full-length mammalian cytochrome b₅ in a membrane environment.
abstract: Microsomal cytochrome b5 plays a key role in the oxidation of a variety of exogenous and endogenous compounds, including drugs, fatty acids, cholesterol and steroid hormones. To better understand its functional properties in a membrane mimic environment, we carried out high-resolution solution NMR studies. Here we report resonance assignments for full-length rabbit cytochrome b5 embedded in dodecylphosphocholine micelles.
authors.affiliation: Department of Chemistry and Biophysics, University of Michigan, Ann Arbor, MI, 48109-1055, USA.
authors.forename: Subramanian
authors.initials: S
authors.lastname: Vivekanandan
authors.forename: Shivani
authors.initials: S
authors.lastname: Ahuja
authors.forename: Sang-Choul
authors.initials: SC
authors.lastname: Im
authors.forename: Lucy
authors.initials: L
authors.lastname: Waskell
authors.forename: Ayyalusamy
authors.initials: A
authors.lastname: Ramamoorthy
mesh_terms: D000818:Animals; D002462:Cell Membrane / Q000737:chemistry / Q000201:enzymology*; D015786:Cytochromes b5 / Q000737:chemistry*; D008823:Micelles; D019906:Nuclear Magnetic Resonance, Biomolecular; D010767:Phosphorylcholine / Q000031:analogs & derivatives / Q000737:chemistry; D011817:Rabbits
chemical_list: D008823:Micelles; D010767:Phosphorylcholine; C028810:dodecylphosphocholine; D015786:Cytochromes b5